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2oex
From Proteopedia
(New page: 200px<br /> <applet load="2oex" size="450" color="white" frame="true" align="right" spinBox="true" caption="2oex, resolution 2.58Å" /> '''Structure of ALIX/A...) |
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| - | [[Image:2oex.gif|left|200px]]<br /> | + | [[Image:2oex.gif|left|200px]]<br /><applet load="2oex" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="2oex" size=" | + | |
caption="2oex, resolution 2.58Å" /> | caption="2oex, resolution 2.58Å" /> | ||
'''Structure of ALIX/AIP1 V Domain'''<br /> | '''Structure of ALIX/AIP1 V Domain'''<br /> | ||
==Overview== | ==Overview== | ||
| - | ALIX/AIP1 functions in enveloped virus budding, endosomal protein sorting, and many other cellular processes. Retroviruses, including HIV-1, SIV, and | + | ALIX/AIP1 functions in enveloped virus budding, endosomal protein sorting, and many other cellular processes. Retroviruses, including HIV-1, SIV, and EIAV, bind and recruit ALIX through YPX(n)L late-domain motifs (X = any residue; n = 1-3). Crystal structures reveal that human ALIX is composed of an N-terminal Bro1 domain and a central domain that is composed of two extended three-helix bundles that form elongated arms that fold back into a "V." The structures also reveal conformational flexibility in the arms that suggests that the V domain may act as a flexible hinge in response to ligand binding. YPX(n)L late domains bind in a conserved hydrophobic pocket on the second arm near the apex of the V, whereas CHMP4/ESCRT-III proteins bind a conserved hydrophobic patch on the Bro1 domain, and both interactions are required for virus budding. ALIX therefore serves as a flexible, extended scaffold that connects retroviral Gag proteins to ESCRT-III and other cellular-budding machinery. |
==About this Structure== | ==About this Structure== | ||
| - | 2OEX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 2OEX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OEX OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Fisher, R | + | [[Category: Fisher, R D.]] |
| - | [[Category: Hill, C | + | [[Category: Hill, C P.]] |
[[Category: Robinson, H.]] | [[Category: Robinson, H.]] | ||
[[Category: Zhai, Q.]] | [[Category: Zhai, Q.]] | ||
[[Category: coiled-coil]] | [[Category: coiled-coil]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:17:40 2008'' |
Revision as of 16:17, 21 February 2008
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Structure of ALIX/AIP1 V Domain
Overview
ALIX/AIP1 functions in enveloped virus budding, endosomal protein sorting, and many other cellular processes. Retroviruses, including HIV-1, SIV, and EIAV, bind and recruit ALIX through YPX(n)L late-domain motifs (X = any residue; n = 1-3). Crystal structures reveal that human ALIX is composed of an N-terminal Bro1 domain and a central domain that is composed of two extended three-helix bundles that form elongated arms that fold back into a "V." The structures also reveal conformational flexibility in the arms that suggests that the V domain may act as a flexible hinge in response to ligand binding. YPX(n)L late domains bind in a conserved hydrophobic pocket on the second arm near the apex of the V, whereas CHMP4/ESCRT-III proteins bind a conserved hydrophobic patch on the Bro1 domain, and both interactions are required for virus budding. ALIX therefore serves as a flexible, extended scaffold that connects retroviral Gag proteins to ESCRT-III and other cellular-budding machinery.
About this Structure
2OEX is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structural and biochemical studies of ALIX/AIP1 and its role in retrovirus budding., Fisher RD, Chung HY, Zhai Q, Robinson H, Sundquist WI, Hill CP, Cell. 2007 Mar 9;128(5):841-52. PMID:17350572
Page seeded by OCA on Thu Feb 21 18:17:40 2008
